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Acquired Immunity
Published in Peter Kam, Ian Power, Michael J. Cousins, Philip J. Siddal, Principles of Physiology for the Anaesthetist, 2020
Peter Kam, Ian Power, Michael J. Cousins, Philip J. Siddal
Two types of light chain, kappa (κ) and lambda (λ), are present in all immunoglobulins. There are five types of heavy chains, α, δ, ε, γ, and μ, produced through gene variation encoding for the heavy chains. These immunoglobulins differ in the amino acid sequence of their heavy chains, in their physical characteristics and in their immunological function (Table 56.2).
Anti-ldiotype Antibodies: Novel Therapeutic Approach to Cancer Therapy
Published in Ronald H. Goldfarb, Theresa L. Whiteside, Tumor Immunology and Cancer Therapy, 2020
Kenneth A. Foon, Malaya Bhattacharya-Chatterjee
Immunoglobulin (Ig) molecules possess variable regions specific for antigen recognition. The variable region is encoded by VH, D and JH genes for the heavy chains and VL and JL chains for the light chain (1). The variable region contains determinants known as idiotypes (Ids), which are themselves immunogenic. Antibodies can be made to many structures in the variable region associated with the light chain, heavy chain, or a combination of both chains (2,3). Early studies by Oudin and Michel (3) and Kunkel and co-workers (2) indicated that an Id was unique to a small set of antibody molecules. However, the idiotypic determinants may show a continuum of specificity from more or less private to semi-public (4,5), e.g., if different antibodies are coded by the same VH gene segment, a shared or semi-public Id may be found. The Id is often defined by the antibody made against it known as anti-Id antibody.
The Lymphatic/Immune System and Its Disorders
Published in Walter F. Stanaszek, Mary J. Stanaszek, Robert J. Holt, Steven Strauss, Understanding Medical Terms, 2020
Walter F. Stanaszek, Mary J. Stanaszek, Robert J. Holt, Steven Strauss
Each Y-shaped antibody or immunoglobulin is made up of two light peptide chains and two heavy chains. The arms of the Y form the variableregion, which differs for each specific antibody; the variable region contains the combining site(antigen-binding site) specific for the antigens to which they attach and can be split chemically to yield the Fab fragment(antigen-binding fragment). There are five different kinds of heavy chains providing the classification of immunoglobulins: IgA (or gA), IgG, IgD, IgE, and IgM.
Antibody markup language (AbML) — a notation language for antibody-based drug formats and software for creating and rendering AbML (abYdraw)
Published in mAbs, 2022
James Sweet-Jones, Maham Ahmad, Andrew C.R. Martin
Consequently, the first line shows the first heavy chain consisting of domains VH, CH1, Hinge, CH2 and CH3 and these are numbered as domains 1–5. The end of the chain is indicated by the |. The second line shows the first light chain (domains VL and CL, numbered as domains 6 and 7). The third line shows the second heavy chain consisting of domains VH, CH1, Hinge, CH2 and CH3 (domain numbers 8–12) while the fourth line shows the second light chain (domains VL and CL, numbered as domains 13 and 14). Domain interactions are shown after colons (e.g., VH.a(1:6) indicates that this domain interacts with domain 6, which is VL.a(6:1)). Hinge region H(3:10){2} shows the interaction with hinge region H(10:3){2} and the {2} indicates that there are two disulfide bonds.
Oligoclonal bands: clinical utility and interpretation cues
Published in Critical Reviews in Clinical Laboratory Sciences, 2022
Sara Carta, Diana Ferraro, Sergio Ferrari, Chiara Briani, Sara Mariotto
Immunoglobulins are formed by two heavy chains, which determine their class (IgG, IgM, IgE, IgD, and IgA) and by two light chains (either kappa or lambda). Light chains are produced in excess of Ig [80], and the intrathecal synthesis of free light chains (FLCs), and in particular of kappa FLCs (KFLCs) is gaining increasing interest as a possibly more sensitive, less costly, less time-consuming, automated, non-operator-dependent, and quantitative marker of intrathecal immunoglobulin synthesis compared to OCB detection [81,82]. Several large studies on the kappa index (CSF/serum KFLC divided by the CSF/serum albumin ratio) showed that the best kappa index cutoff for predicting MS is between 5.9 and 6.6 [81–83]. The higher sensitivity of the kappa index compared to CSF OCBs was underlined in a large cohort of OCB-negative MS patients (n = 92), in whom one quarter had an elevated kappa index [84]. However, its higher sensitivity comes at expense of a lower specificity [81–83].
Keeping up with venetoclax for leukemic malignancies: key findings, optimal regimens, and clinical considerations
Published in Expert Review of Clinical Pharmacology, 2021
Maria Siddiqui, Marina Konopleva
Venetoclax has changed treatment paradigms in hematological malignancies particularly acute myeloid leukemia (AML) and chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL). It is currently the subject of over a hundred investigational trials as a single or a combination agent. Venetoclax, a selective BH3 mimetic, works through targeting the arbitrator of apoptosis, the B-cell leukemia/lymphoma-2 (BCL-2) protein [1]. In addition to potent efficacy, the favorable toxicity profile and ease of administration have enhanced its success. BCL-2 was initially discovered as part of the translocation (14;18) in follicular lymphoma [2, 3]. Being a counterpart to the immunoglobulin heavy-chain locus, it was believed to cause cellular proliferation until studies later elucidated its key role in apoptosis [4]. In the landmark paper ‘Hallmarks of Cancer,’ Hanahan and Weinberg proposed six mechanisms shared among all human tumors with one of them being evasion of apoptosis [5]. This substantiated the notion that oncogenesis together with excessive proliferation is further driven by the avoidance of cell death. The overexpression of BCL-2 family proteins plays a key role in apoptotic evasion and targeting these proteins became an alluring prospect to regulate and halt tumor growth.